ID   DLDH3_BACSU             Reviewed;         458 AA.
AC   O34324;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 81.
DE   RecName: Full=Dihydrolipoyl dehydrogenase;
DE            EC=1.8.1.4;
DE   AltName: Full=Dihydrolipoamide dehydrogenase;
DE   AltName: Full=E3 component of acetoin cleaving system;
GN   Name=acoL; Synonyms=yfjH; OrderedLocusNames=BSU08090;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=99296597; PubMed=10368162;
RA   Huang M., Oppermann-Sanio F.B., Steinbuchel A.;
RT   "Biochemical and molecular characterization of the Bacillus subtilis
RT   acetoin catabolic pathway.";
RL   J. Bacteriol. 181:3837-3841(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / AC327;
RX   MEDLINE=97124190; PubMed=8969503;
RA   Yamamoto H., Uchiyama S., Sekiguchi J.;
RT   "Cloning and sequencing of a 40.6 kb segment in the 73 degrees-76
RT   degrees region of the Bacillus subtilis chromosome containing genes
RT   for trehalose metabolism and acetoin utilization.";
RL   Microbiology 142:3057-3065(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
CC   -!- CATALYTIC ACTIVITY: Protein N(6)-(dihydrolipoyl)lysine + NAD(+) =
CC       protein N(6)-(lipoyl)lysine + NADH.
CC   -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC   -!- PATHWAY: Ketone degradation; acetoin degradation.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family.
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DR   EMBL; AF006075; AAC05585.1; -; Genomic_DNA.
DR   EMBL; D78509; BAA24293.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12638.1; -; Genomic_DNA.
DR   PIR; G69581; G69581.
DR   RefSeq; NP_388690.1; -.
DR   HSSP; P14218; 1LPF.
DR   GeneID; 939702; -.
DR   GenomeReviews; AL009126_GR; BSU08090.
DR   KEGG; bsu:BSU08090; -.
DR   NMPDR; fig|224308.1.peg.809; -.
DR   SubtiList; BG12561; ACOL.
DR   HOGENOM; O34324; -.
DR   OMA; O34324; KAGIQYS.
DR   BioCyc; BSUB224308:BSU0809-MON; -.
DR   BRENDA; 1.8.1.4; 150.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:EC.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0045150; P:acetoin catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR000815; Hg_reductase.
DR   InterPro; IPR006258; Lipoamide_DH.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   InterPro; IPR001327; Pyr_OxRdtase_NAD_bd.
DR   Gene3D; G3DSA:3.30.390.30; Pyr_redox_dim; 1.
DR   PANTHER; PTHR22912:SF20; Lipoamide_DH; 1.
DR   Pfam; PF00070; Pyr_redox; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00945; HGRDTASE.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
DR   TIGRFAMs; TIGR01350; lipoamide_DH; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   3: Inferred from homology;
KW   Acetoin catabolism; Complete proteome; Cytoplasm; Disulfide bond; FAD;
KW   Flavoprotein; Glycolysis; NAD; Oxidoreductase; Redox-active center.
FT   CHAIN         1    458       Dihydrolipoyl dehydrogenase.
FT                                /FTId=PRO_0000068018.
FT   NP_BIND      30     38       FAD (By similarity).
FT   NP_BIND     177    181       NAD (By similarity).
FT   NP_BIND     263    266       NAD (By similarity).
FT   ACT_SITE    437    437       Proton acceptor (By similarity).
FT   BINDING      47     47       FAD (By similarity).
FT   BINDING     112    112       FAD; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING     200    200       NAD (By similarity).
FT   BINDING     305    305       FAD (By similarity).
FT   BINDING     313    313       FAD; via amide nitrogen (By similarity).
FT   DISULFID     38     43       Redox-active (By similarity).
SQ   SEQUENCE   458 AA;  48853 MW;  2496832534945183 CRC64;
     MTLAIIGGGP AGYAAAVSAA QQGRNVLLID KGKLGGTCLN EGCIPTKSLL ESANVLDKIK
     HADSFGIELP AGAISVDWSK MQSRKQQVVS QLVQGVQYLM KKNQIQVVKG TASFLSERKL
     LIEGENGKEI READQVLIAS GSEPIELPFA PFDGEWILDS KDALSLSEIP SSLVIVGGGV
     IGCEYAGLFA RLGSQVTIIE TADRLIPAED EDIARLFQEK LEEDGVEVHT SSRLGRVDQT
     AKTAIWKSGQ REFKTKADYV LVAIGRKPRL DGLQLEQAGV DFSPKGIPVN GHMQTNVPHI
     YACGDAIGGI QLAHAAFHEG IIAASHASGR DVKINEKHVP RCIYTSPEIA CIGMTERQAR
     SIYGDVKIGE FSFSANGKAL IKQQAEGKVK IMAEPEFGEI VGVSMIGPDV TELIGQAAAI
     MNGEMTADMA EHFIAAHPTL SETLHEALLS TIGLAVHA
//